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Titlebook: Biomolecular Structure and Dynamics; Gérard Vergoten,Theophile Theophanides Book 1997 Springer Science+Business Media Dordrecht 1997 Pepti

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期刊全稱Biomolecular Structure and Dynamics
影響因子2023Gérard Vergoten,Theophile Theophanides
視頻videohttp://file.papertrans.cn/189/188261/188261.mp4
學(xué)科分類NATO Science Series E:
圖書封面Titlebook: Biomolecular Structure and Dynamics;  Gérard Vergoten,Theophile Theophanides Book 1997 Springer Science+Business Media Dordrecht 1997 Pepti
影響因子.Biomolecular Structure and Dynamics. describes recentfundamental advances in the experimental and theoretical study ofmolecular dynamics and stochastic dynamic simulations, X-raycrystallography and NMR of biomolecules, the structure of proteins andits prediction, time resolved Fourier transform IR spectroscopy ofbiomolecules, the computation of free energy, applications ofvibrational CD of nucleic acids, and solid state NMR. Furtherpresentations include recent advances in UV resonance Ramanspectroscopy of biomolecules, semiempirical MO methods, empiricalforce fields, quantitative studies of the structure of proteins inwater by Fourier transform IR, and density functional theory.Metal-ligand interactions, DFT treatment of organometallic andbiological systems, and simulation vs. X-ray and far IR experimentsare also discussed in some detail. .The book provides a broad perspective of the current theoreticalaspects and recent experimental findings in the field of biomoleculardynamics, revealing future research trends, especially in areas wheretheoreticians and experimentalists could fruitfully collaborate.
Pindex Book 1997
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Approaches to Protein-Ligand Binding from Computer Simulationsations of statistical mechanics simulations to the problem are considered that feature full atomic-level descriptions of the protein, ligand and aqueous environment. Basic concepts on the methodology and intermolecular interactions in solution are presented along with results of Monte Carlo simulati
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Dynamics of Biomolecules : Simulation Versus X-Ray and Far-Infrared Experimentsular mobility [1]. In many areas of molecular biology, such as muscle contraction or conformational changes in allosteric proteins, motion is self-evidently crucial. In facilitating such processes as the access of ligands to protein binding sites or in accomodating the change in protein and substrat
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Professional Gamblingortance for the design of drugs. Structural information often greatly enhances our understanding of how proteins function and how they interact with each other or it can, for example, explain antigenic behaviour, DNA binding specificity, etc. X-ray crystallography and NMR spectroscopy are the only w
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Biomolecular Structure and Dynamics: Recent Experimental and Theoretical Advances study of biomolecules in solution, thus closer to their real physiological environment. The method is limited, however, to biomolecules of relatively small size due to limitations in spectral resolution and line broadening effects. The upper limit is presently situated around molecular weights of 3
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What Drives Association of α-Helical Peptides in Membrane Domains of Proteins? Role of Hydrophobic Ipore-forming proteins. Their hydrophobic and packing properties were analyzed using Monte Carlo simulations in solvents of different polarity, molecular hydrophobicity potential calculations and environmental profiles method. The results obtained in independent techniques are in reasonable agreement
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